Pamela R. Hall, Ph.D.

Molecular Genetics and Microbiology
MSC08 4660
1 University of New Mexico
Albuquerque, NM 87131-0001
 
Office: BMSB 385
Tel: (505) 272-4210
Fax: (505) 272-6029
E-mail: phall@salud.unm.edu

Keywords: Methicillin-resistant Staphylococcus aureus (MRSA), apolipoprotein B, innate immunity, quorum sensing, peptide therapeutics

Research Interests

With a background in pharmacology and protein structure determination using X-ray crystallography, I have a keen interest in understanding protein-protein and protein-peptide interactions and how these can be exploited for therapeutics. Protein-protein interactions are crucial for a multitude of cellular processes, not the least of which includes our immune response to pathogens. My current work focuses on how our innate immune system utilizes such interactions in defending us against invasive infection by methicillin-resistant Staphylococcus aureus (MRSA). MRSA, both community-acquired and hospital-acquired, has recently been highlighted in the press due to its impact on both public health and on the added financial burden to patient care. S. aureus utilizes a peptide-pheromone based communication system, called quorum-sensing, to switch from an adherent phenotype to one capable of invasive infection. The peptide pheromones responsible for signaling this change in virulence are referred to as autoinducing peptides or AIPs. It has recently been discovered that apolipoprotein B (apoB), a component of both very-low density lipoprotein (VLDL) and low density lipoprotein (LDL) particles, can bind to AIPs and prevent the switch to an invasive bacterial phenotype. We are currently working to understand the complete mechanism by which apoB antagonizes quorum sensing. This information will provide insight into the role of this molecule as an innate defense protein and possibly provide clues to identification of therapeutic inhibitors of MRSA quorum sensing.

Selected Publications

Peterson, M.M., Mack, J.L., Hall, P.R., Alsup, A.A., Alexander, S.M., Sully, E.K., Sawires, Y.S., Cheung, A.L., Otto, M. and Gresham, H.D. (2008) Apolipoprotein B is an Innate Barrier Against Invasive Staphylococcus aureus Infection. Cell Host and Microbe. 4:555-566.

Hall, P.R., Hjelle, B., Brown, D.C., Ye, C., Bondu-Hawkins, V., Kilpatrick, K.A. and Larson, R.S. (2008) Multivalent presentation of anti-hantavirus peptides on nanoparticles enhances infection blockade. Antimicrobial Agents and Chemotherapy, 52:2079-2088.

HALL PR, Malone L, Sillerud LO, Ye C, Hjelle B and Larson RS. Characterization and NMR solution structure of a novel cyclic pentapeptide inhibitor of pathogenic hantaviruses. Chemical Biology & Drug Design, 69:180-190, 2007.

Prescott J, HALL PR, Bondu-Hawkins V, Ye C and Hjelle B. Early Innate Immune Responses to Sin Nombre Hantavirus Occur Independently of IFN Regulatory Factor 3, Characterized Pattern Recognition Receptors, and Viral Entry. J. Immunology, 179:1796-1802, 2007.

Bell JK, Askins J, HALL PR, Davies DR and Segal DM. The dsRNA binding site of human Toll-like receptor 3. Proc. Natl. Acad. Sci. USA 103:8792-8797, 2006.

Bell, J.K., Botos, I., Hall, P.R., Askins, J., Shiloach, J., Davies, D.R. and Segal, D.M. The molecular structure of the TLR3 extracellular domain. J Endotoxin Res. 12:375-378, 2006.

Bell JK, Botos I, HALL PR, Askins J, Shiloach J, Segal DM, and Davies DR. The molecular structure of the Toll-like receptor 3 ligand-binding domain. Proc. Natl. Acad. Sci. USA 102:10976-10980, 2005.

HALL PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR. and Yee VC. Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit. EMBO J 23: 3621-3631, 2004.

HALL PR, Zheng R, Pusztai-Carey M, van den Akker F, Carey PR, and Yee VC. Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit. Acta. Crystallogr. D. 60:521-523, 2004.

HALL PR, Wang Y-F, Rivera-Hainaj RE, Zheng X, Pusztai-Carey M, Carey PR, and Yee VC. Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core. EMBO J. 22:2334-2347, 2003.